抗Mouse Chemerin Biotinylated抗体(Anti-Mouse Chemerin Biotinylated antibody)
掲載日情報:2021/01/28 現在Webページ番号:195219
Mouse Chemerin Biotinylatedに対する抗体(Anti-Mouse Chemerin Biotinylated )です。
※ 本製品は研究用です。研究用以外には使用できません。
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- 価格
- Product Details
- Applications and Data
- References
- Related Research Areas
- Related Product & Information
価格
[在庫・価格 :2024年04月30日 09時55分現在]
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Anti-Mouse Chemerin Biotinylated MAb (Clone 372402) |
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[在庫・価格 :2024年04月30日 09時55分現在]
Anti-Mouse Chemerin Biotinylated MAb (Clone 372402)
文献数: 0
- 商品コード:BAM2325
- メーカー:RSD
- 包装:250μg
- 価格:¥118,000
- 在庫:無(未発注)
- 納期:10日程度 ※※ 表示されている納期は弊社に在庫がなく、取り寄せた場合の目安納期となります。
- 法規制等:
説明文 |
マッチドペア:Mouse Chemerin サンドイッチELISAの検出用抗体として利用可能,補足用抗体として#MAB23251,スタンダードとして#2325-CM-025を用いる。 別名:chemerin クローン:372402 Genbank No: 5919 Protein Accession No: Q9DD06 |
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法規制等 | |||
保存条件 | -20℃ | 法規備考 | |
抗原種 | 免疫動物 | Rat | |
交差性 | Mouse | 適用 | ELISA |
標識 | Biotin | 性状 | Protein A/G Affinity Purified |
吸収処理 | クラス | IgG | |
クロナリティ | Monoclonal | フォーマット | |
掲載カタログ |
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製品記事 |
MagCellect™ Mouse and Human Natural Killer Cell Isolation Kits |
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関連記事 |
R&D Systems(R&Dシステムズ)社 ELISA用ペア抗体を使用したELISA 構築ガイド |
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Product Details
Species Reactivity | Mouse |
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Label | Biotin |
Immunogen | E. coli-derived recombinant mouse ChemerinThr17-Ser156Accession # Q9DD06 |
Source | Monoclonal Rat IgG2A Clone # 372402 |
Purification | Protein A or G purified from hybridoma culture supernatant |
Specificity | Detects mouse Chemerin in ELISAs. In sandwich immunoassays, no cross-reactivity or interference with recombinant human Chemerin, recombinant mouse (rm) Cystatin C, or rmFetuin A is observed. |
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Applications and Data
Recommended Concentration | Sample | |
Mouse Chemerin Sandwich Immunoassay | Reagent | |
ELISA Capture (Matched Antibody Pair) | 2-8 µg/mL | Mouse Chemerin Antibody (Catalog #MAB23251 ) |
ELISA Detection (Matched Antibody Pair) | 0.5-2.0 µg/mL | Mouse Chemerin Biotinylated Antibody (Catalog #BAM2325 ) |
ELISA Standard | Recombinant Mouse Chemerin (aa 17-156) Protein (Catalog #2325-CM ) | |
Please Note: Optimal dilutions should be determined by each laboratory for each application.General Protocolsare available in the Technical Information section on our website. | Preparation and Storage | |
Reconstitution | Reconstitute at 0.5 mg/mL in sterile PBS. | Reconstitution Buffer Available |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | |
Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. | |
1 month, 2 to 8 °C under sterile conditions after reconstitution. | ||
6 months, -20 to -70 °C under sterile conditions after reconstitution. | ||
Background: Chemerin | Mouse Chemerin, also known as Tazarotene-induced Gene-2 (TIG2), is a new, but distant member of the cystatin superfamily (1‑3). Members of this superfamily contain at least two intrachain disulfide bonds and an alpha -helical structure over a distance of about 100 amino acids (aa) (2, 3). Chemerin is synthesized as a 162 aa precursor that contains a hydrophobic N-terminal sequence, an intervening 140 aa cystatin-fold containing domain, and a six aa C-terminal prosegment (4‑6). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the characteristic fold (4, 7). The precursor molecule is described as undergoing proteolytic processing at both termini by unknown proteases. The N-terminal 16 residue hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (5, 8). In either case it gives rise to a soluble proform that undergoes further processing at the C-terminus (5). In mouse, the C-terminal six residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 17‑156) (5‑7). A shorter form has been described in human (7). The activity seems to be concentrated in the nine aa’s preceding the prosegment (aa 148‑156). Retention of the prosegment blocks activity (4). The 140 aa mature segment is known to bind to the G-protein coupled receptor termed ChemR23 (5, 7). Binding results in macrophage and immature dendritic cell chemotaxis (5). The distribution of this receptor is limited to immune APCs, and it is assumed that Chemerin is an inflammatory molecule. It is unclear which cells are actually producing Chemerin, but keratinocytes, endothelial cells and osteoclasts are potential candidates (1, 7). Mature mouse Chemerin shares 67%, 84% and 82% aa sequence identity with human, rat and hamster Chemerin, respectively (6). There is apparently cross-species activity for the protein (6). |
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References
Nagpal, S. et al. (1997) J. Invest. Dermatol. 109:91. | |
Storici, P. et al. (1996) Eur. J. Biochem. 238:769. | |
Zanetti, M. (2004) J. Leukoc. Biol. 75:39. | |
Wittamer, V. et al. (2004) J. Biol. Chem. 279:9956. | |
Wittamer, V. et al. (2003) J. Exp. Med. 198:977. | |
Busmann, A. et al. (2004) J. Chromatog. B 811:217. | |
Meder, W. et al. (2003) FEBS Lett. 555:495. | |
Yokoyama-Kobayashi, M. et al. (1999) Gene 228:161. | |
Long Name: | Retinoic Acid Receptor Responder Protein 2 |
Entrez Gene IDs: | 5919 (Human); 71660 (Mouse) |
Alternate Names: | Chemerin; RARRES2; RAR-responsive protein TIG2; retinoic acid receptor responder (tazarotene induced) 2; retinoic acid receptor responder protein 2; Tazarotene-induced gene 2 protein; TIG-2; TIG2HP10433 |
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Related Research Areas
Adipocytokines |
Inflammatory Mediators |
Other Chemokine-related Ligands and Receptors |
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Related Product & Information
Background | Chemerin |
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background_content | Background: Chemerin Mouse Chemerin, also known as Tazarotene-induced Gene-2 (TIG2), is a new, but distant member of the cystatin superfamily (1‑3). Members of this superfamily contain at least two intrachain disulfide bonds and an alpha -helical structure over a distance of about 100 amino acids (aa) (2, 3). Chemerin is synthesized as a 162 aa precursor that contains a hydrophobic N-terminal sequence, an intervening 140 aa cystatin-fold containing domain, and a six aa C-terminal prosegment (4‑6). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the characteristic fold (4, 7). The precursor molecule is described as undergoing proteolytic processing at both termini by unknown proteases. The N-terminal 16 residue hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (5, 8). In either case it gives rise to a soluble proform that undergoes further processing at the C-terminus (5). In mouse, the C-terminal six residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 17‑156) (5‑7). A shorter form has been described in human (7). The activity seems to be concentrated in the nine aa’s preceding the prosegment (aa 148‑156). Retention of the prosegment blocks activity (4). The 140 aa mature segment is known to bind to the G-protein coupled receptor termed ChemR23 (5, 7). Binding results in macrophage and immature dendritic cell chemotaxis (5). The distribution of this receptor is limited to immune APCs, and it is assumed that Chemerin is an inflammatory molecule. It is unclear which cells are actually producing Chemerin, but keratinocytes, endothelial cells and osteoclasts are potential candidates (1, 7). Mature mouse Chemerin shares 67%, 84% and 82% aa sequence identity with human, rat and hamster Chemerin, respectively (6). There is apparently cross-species activity for the protein (6). |
追加しました。
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